Imaging the membrane protein bacteriorhodopsin with the atomic force microscope.
The membrane protein bacteriorhodopsin was imaged in buffer solution at room temperature with the atomic force microscope. Three different substrates were used: mica, silanized glass and lipid bilayers. Single bacteriorhodopsin molecules could be imaged in purple membranes adsorbed to mica. A depression was observed between the bacteriorhodopsin molecules. The two dimensional Fourier transform showed the hexagonal lattice with a lattice constant of 6.21 +/- 0.20 nm which is in agreement with results of electron diffraction experiments. Spots at a resolution of approximately 1.1 nm could be resolved. A protein, cationic ferritin, could be imaged bound to the purple membranes on glass which was silanized with aminopropyltriethoxysilane. This opens the possibility of studying receptor/ligand binding under native conditions. In addition, purple membranes bound to a lipid bilayer were imaged. These images may help in interpreting results of functional studies done with purple membranes adsorbed to black lipid membranes.
Butt
H J
HJ
Department of Physics, University of California, Santa Barbara 93106.
Downing
K H
KH
Hansma
P K
PK
D000327:Adsorption; D000538:Aluminum Silicates; D001436:Bacteriorhodopsins / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure*; D004577:Electron Probe Microanalysis / Q000295:instrumentation / Q000379:methods; D005293:Ferritins / Q000378:metabolism; D005898:Glass; D008051:Lipid Bilayers; D011485:Protein Binding
D000538:Aluminum Silicates; D008051:Lipid Bilayers; D001436:Bacteriorhodopsins; D005293:Ferritins; C011934:mica